Characterization of a novel hormone-sensitive lipase family esterase from Rhizomucor miehei with tertiary alcohol hydrolysis activity

Yan, Qiaojuan; Yang, Shaoqing; Duan, Xiaojie; Xu, Hui; Liu, Yu; Jiang, Zhengqiang

doi:10.1016/j.molcatb.2014.08.008

Cited by 17 publications

(31 citation statements)

References 44 publications

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“…(Dou et al., ; Ngo et al., ; Palm et al., ; Wei et al., ), only two HSL have been biochemically studied and crystallized in fungi (PDBs 4WY8 and 4WY5) (Yang, Qin, et al., ). 4WY8 and 4WY5 are the crystal structures of Rm EstB and Rm EstA, respectively, both esterases belonging to a member of the order Mucorales (Liu et al., ; Yan et al., ; Yang, Qin, et al., ). The structural alignments with the previous fungal HSL allowed identifying the cap (purple) and the catalytic domains (green) in Ba EstB (Figure a), as well as the catalytic triad, which was located in the respective canonical position.…”

Section: Resultsmentioning

confidence: 99%

“…Incubation at 10°C to 30°C showed around 97% of its activity, whereas incubation at 50°C abolished the activity to 5% (Figure b). HSL counterparts in Rhizomucor show similar optimal temperatures between 45 and 50°C (Liu et al., ; Yan et al., ), while other esterases from metagenomic libraries have their optimal temperatures around 30°C (Jeon et al., ; Li et al., , ). Considering the temperature, Ba EstB is a mesophilic HSL esterase, compared with a thermostable esterase from Thermoanaerobacter tengcongensis with optimal temperature at 70°C (Rao et al., ).…”

Section: Resultsmentioning

confidence: 99%

“…The effect of several detergents (Tween 20, Tween 80, SDS, Triton X‐100, and CTAB) and EDTA on the Ba EstB activity was evaluated. Residual activity, expressed in percentage, was calculated by incubating the Ba EstB in Tris‐HCl buffer for 1 hr at 30°C in presence of 5% ( w/v ) of each compound (Yan et al., ).…”

Section: Methodsmentioning

confidence: 99%

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The first description of a hormone‐sensitive lipase from a basidiomycete: Structural insights and biochemical characterization revealed Bjerkandera adusta BaEstB as a novel esterase

et al. 2017

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The heterologous expression and characterization of a Hormone‐Sensitive Lipases (HSL) esterase (BaEstB) from the Basidiomycete fungus Bjerkandera adusta is reported for the first time. According to structural analysis, amino acid similarities and conservation of particular motifs, it was established that this enzyme belongs to the (HSL) family. The cDNA sequence consisted of 969 nucleotides, while the gene comprised 1133, including three introns of 57, 50, and 57 nucleotides. Through three‐dimensional modeling and phylogenetic analysis, we conclude that BaEstB is an ortholog of the previously described RmEstB‐HSL from the phylogenetically distant fungus Rhizomucor miehei. The purified BaEstB was characterized in terms of its specificity for the hydrolysis of different acyl substrates confirming its low lipolytic activity and a noticeable esterase activity. The biochemical characterization of BaEstB, the DLS analysis and the kinetic parameters determination revealed this enzyme as a true esterase, preferentially found in a dimeric state, displaying activity under alkaline conditions and relative low temperature (pH = 10, 20°C). Our data suggest that BaEstB is more active on substrates with short acyl chains and bulky aromatic moieties. Phylogenetic data allow us to suggest that a number of fungal hypothetical proteins could belong to the HSL family.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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The first description of a hormone‐sensitive lipase from a basidiomycete: Structural insights and biochemical characterization revealed Bjerkandera adusta BaEstB as a novel esterase

et al. 2017

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“…However, it was not possible to maintain this pH, since the change resulted in enzyme precipitation, which can be explained by the fact that this enzyme has a higher activity in alkaline conditions, between pH 6.0 and 10.0 being optimal. 26,44 Therefore, the model solutions for the enzyme application in trichothecene degradation assays were established as phosphate buffer 0.05 mol L -1 at pH 5.0 for laccase and at pH 7.0 for lipase.…”

Section: Enzymatic Activity Standardizationmentioning

confidence: 99%

Evaluation of the Suitability of Analytical Methods in Trichothecene A and B Degradation

Feltrin

Sibaja

Tusnski

et al. 2018

J. Braz. Chem. Soc.

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An investigation was conducted to standardize conditions for laccase and lipase activity required to maximize trichothecene degradation. The analytical methods were suitable and validated in model solutions for detection of five analytes (T-2 toxin, deoxynivalenol, nivalenol, 3-acetyldeoxynivalenol and 15-acetyldeoxynivalenol), the methods were then applied in the degradation tests of these trichothecenes. The method of salting-out assisted liquid-liquid extraction (SALLE), using three different NaCl concentration levels, obtained recoveries in the range of 47.4-103.4% at pH 5.0 and 36.6-106.8% at pH 7.0, with an intra-day relative standard deviation under 15% for the majority of the compounds. Quantification limits remained in the region of 0.07 μg mL -1 for 15-acetyldeoxynivalenol and 0.3 μg mL -1 for nivalenol. Finally, the suitable analytical methods were applied in a study of trichothecene degradation by enzymatic action, resulting in a reduction of 12.3% for T-2 toxin, 68.4% for deoxynivalenol, 50.2% for 3-acetyldeoxynivalenol and 45.4% for 15-acetyldeoxynivalenol.

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“…The great commercial importance of lipases is due to their wide range of applications in detergents, pharmaceuticals, foods (cheese and tea), pulp and paper, textiles, tanneries, cosmetics, biodiesel and wastewater treatment (Messias et al, 2011;Roveda et al, 2010;Yan et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

LIPASE PRODUCTION BY Aspergillus niger GROWN IN DIFFERENT AGRO-INDUSTRIAL WASTES BY SOLID-STATE FERMENTATION

Costa

Hermann

García-Román

et al. 2017

Braz. J. Chem. Eng.

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-Filamentous fungi can easily degrade agro-industrial wastes in solid-state fermentation processes, synthesizing many important commercial biocompounds, such as lipolytic enzymes. The aim of this study was to evaluate the effect of the composition of the solid culture medium on the production of lipolytic enzymes by the fungus Aspergillus niger. Rice, wheat and soybean bran were mixed to prepare the culture medium, which was supplemented with glucose, glycerol or soybean oil. Four mixture experimental designs were used to find the best medium for enzyme production. According to our results, the highest lipolytic activity values were achieved with a mixture of rice bran and glycerol (19.844 U·g -1 ) or with rice bran only (13.267 U·g -1 ). Thus, the lipolytic enzyme could be produced without any additional carbon source apart from rice bran, although glycerol addition induced a higher production.

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Characterization of a novel hormone-sensitive lipase family esterase from Rhizomucor miehei with tertiary alcohol hydrolysis activity

Cited by 17 publications

References 44 publications

The first description of a hormone‐sensitive lipase from a basidiomycete: Structural insights and biochemical characterization revealed Bjerkandera adusta BaEstB as a novel esterase

The first description of a hormone‐sensitive lipase from a basidiomycete: Structural insights and biochemical characterization revealed Bjerkandera adusta BaEstB as a novel esterase

Evaluation of the Suitability of Analytical Methods in Trichothecene A and B Degradation

LIPASE PRODUCTION BY Aspergillus niger GROWN IN DIFFERENT AGRO-INDUSTRIAL WASTES BY SOLID-STATE FERMENTATION

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